pubmed-article:8359524 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8359524 | lifeskim:mentions | umls-concept:C1521970 | lld:lifeskim |
pubmed-article:8359524 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
pubmed-article:8359524 | lifeskim:mentions | umls-concept:C1415464 | lld:lifeskim |
pubmed-article:8359524 | lifeskim:mentions | umls-concept:C0063110 | lld:lifeskim |
pubmed-article:8359524 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
pubmed-article:8359524 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:8359524 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:8359524 | pubmed:dateCreated | 1993-9-30 | lld:pubmed |
pubmed-article:8359524 | pubmed:abstractText | The mechanism that has been proposed for glyoxalase II [36] is summarized in Figure 3. It involves direct nucleophilic attack of an active-site histidine on the thiol ester substrate to form an acyl-imidazole intermediate which then rapidly hydrolyses. This is consistent with the known susceptibility of thiol esters to aminolysis and with the lability of acyl-imidazoles [47]. | lld:pubmed |
pubmed-article:8359524 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8359524 | pubmed:language | eng | lld:pubmed |
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pubmed-article:8359524 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8359524 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8359524 | pubmed:month | May | lld:pubmed |
pubmed-article:8359524 | pubmed:issn | 0300-5127 | lld:pubmed |
pubmed-article:8359524 | pubmed:author | pubmed-author:Vander... | lld:pubmed |
pubmed-article:8359524 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8359524 | pubmed:volume | 21 | lld:pubmed |
pubmed-article:8359524 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8359524 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8359524 | pubmed:pagination | 522-7 | lld:pubmed |
pubmed-article:8359524 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:8359524 | pubmed:meshHeading | pubmed-meshheading:8359524-... | lld:pubmed |
pubmed-article:8359524 | pubmed:meshHeading | pubmed-meshheading:8359524-... | lld:pubmed |
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pubmed-article:8359524 | pubmed:meshHeading | pubmed-meshheading:8359524-... | lld:pubmed |
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pubmed-article:8359524 | pubmed:meshHeading | pubmed-meshheading:8359524-... | lld:pubmed |
pubmed-article:8359524 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8359524 | pubmed:articleTitle | Glyoxalase II: molecular characteristics, kinetics and mechanism. | lld:pubmed |
pubmed-article:8359524 | pubmed:affiliation | Department of Biochemistry, University of New Mexico School of Medicine, Albuquerque 87131. | lld:pubmed |
pubmed-article:8359524 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8359524 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8359524 | pubmed:publicationType | Review | lld:pubmed |
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